5lup

X-ray diffraction
2.03Å resolution

Structures of DHBN domain of human BLM helicase

Released:

Function and Biology Details

Reaction catalysed:
ATP + H(2)O = ADP + phosphate
Sequence domain:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
hetero dimer
PDBe Complex ID:
PDB-CPX-156947 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
RecQ-like DNA helicase BLM Chains: A, B, C, D, E, F, G, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, I, J, K, L
Length: 54 amino acids
Theoretical weight: 6.39 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P54132 (Residues: 362-414; Coverage: 4%)
Gene names: BLM, RECQ2, RECQL3
Sequence domains: BDHCT (NUC031) domain
RecQ-like DNA helicase BLM Chain: H
Molecule details ›
Chain: H
Length: 54 amino acids
Theoretical weight: 6.39 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P54132 (Residues: 362-414; Coverage: 4%)
Gene names: BLM, RECQ2, RECQL3
Sequence domains: BDHCT (NUC031) domain

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL18U1
Spacegroup: P62
Unit cell:
a: 132.795Å b: 132.795Å c: 64.984Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.213 0.21 0.263
Expression system: Escherichia coli BL21